Q17745 (TRXR1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 1
Short name=TR-Se
Short name=TRR
EC=1.8.1.9

Gene names

Name:	trxr-1
ORF Names:	C06G3.7

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	667 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Contains a selenide-sulfide bond between Cys-665 and Sec-666. This bond is speculated to serve as redox active pair By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Selenocysteine
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro disulfide oxidoreductase activity Non-traceable author statement. Source: UniProtKB flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 667	667	Thioredoxin reductase 1		PRO_0000067980
Regions
	Nucleotide binding	202 – 219	18	FAD By similarity
Sites
	Active site	639	1	Proton acceptor By similarity
Amino acid modifications
	Non-standard residue	666	1	Selenocysteine
	Disulfide bond	219 ↔ 224		Redox-active By similarity
	Cross-link	665 ↔ 666		Cysteinyl-selenocysteine (Cys-Sec) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q17745 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: 58B86D4274E4FA77	FASTA	667	74,263
	10 20 30 40 50 60 MKSLTELFGC FKRQPRQQEA SSPANPHVSD TLSMGVAASG MPPPKRPAPA ESPTLPGETL 70 80 90 100 110 120 VDAPGIPLKE ALKEAANSKI VIFYNSSDEE KQLVEFETYL NSLKEPADAE KPLEIPEIKK 130 140 150 160 170 180 LQVSRASQKV IQYLTLHTSW PLMYIKGNAV GGLKELKALK QDYLKEWLRD HTYDLIVIGG 190 200 210 220 230 240 GSGGLAAAKE ASRLGKKVAC LDFVKPSPQG TSWGLGGTCV NVGCIPKKLM HQASLLGHSI 250 260 270 280 290 300 HDAKKYGWKL PEGKVEHQWN HLRDSVQDHI ASLNWGYRVQ LREKTVTYIN SYGEFTGPFE 310 320 330 340 350 360 ISATNKKKKV EKLTADRFLI STGLRPKYPE IPGVKEYTIT SDDLFQLPYS PGKTLCVGAS 370 380 390 400 410 420 YVSLECAGFL HGFGFDVTVM VRSILLRGFD QDMAERIRKH MIAYGMKFEA GVPTRIEQID 430 440 450 460 470 480 EKTDEKAGKY RVFWPKKNEE TGEMQEVSEE YNTILMAIGR EAVTDDVGLT TIGVERAKSK 490 500 510 520 530 540 KVLGRREQST TIPWVYAIGD VLEGTPELTP VAIQAGRVLM RRIFDGANEL TEYDQIPTTV 550 560 570 580 590 600 FTPLEYGCCG LSEEDAMMKY GKDNIIIYHN VFNPLEYTIS ERMDKDHCYL KMICLRNEEE 610 620 630 640 650 660 KVVGFHILTP NAGEVTQGFG IALKLAAKKA DFDRLIGIHP TVAENFTTLT LEKKEGDEEL QASGCUG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Selenocysteine-containing thioredoxin reductase in C. elegans." Gladyshev V.N., Krause M., Xu X.-M., Korotkov K.V., Kryukov G.V., Sun Q.-A., Lee B.J., Wootton J.C., Hatfield D.L. Biochem. Biophys. Res. Commun. 259:244-249(1999) [PubMed: 10362494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROBABLE PRESENCE OF A SELENOCYSTEINE.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"The Caenorhabditis elegans homologue of thioredoxin reductase contains a selenocysteine insertion sequence (SECIS) element that differs from mammalian SECIS elements but directs selenocysteine incorporation." Buettner C., Harney J.W., Berry M.J. J. Biol. Chem. 274:21598-21602(1999) [PubMed: 10419466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 143-667, PROBABLE SELENOCYSTEINE AT SEC-666. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF148217 mRNA. Translation: AAD41826.1. FO080396 Genomic DNA. Translation: CCD83555.1. AF162693 mRNA. Translation: AAD46625.1.
PIR	T30091.
RefSeq	NP_501085.2. NM_068684.5.
UniGene	Cel.18219.
3D structure databases
ProteinModelPortal	Q17745.
SMR	Q17745. Positions 69-667.
ModBase	Search...
Proteomic databases
PRIDE	Q17745.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C06G3.7; C06G3.7; C06G3.7.
GeneID	177466.
KEGG	cel:C06G3.7.
UCSC	C06G3.7. c. elegans.
Organism-specific databases
CTD	31760.
WormBase	C06G3.7; CE34250; WBGene00015553; trxr-1.
Phylogenomic databases
eggNOG	meNOG04112.
HOGENOM	HBG515043.
InParanoid	Q17745.
OMA	HPVCAEI.
PhylomeDB	Q17745.
Gene expression databases
ArrayExpress	Q17745.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR012336. Thioredoxin-like_fold. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K00384.
PANTHER	PTHR22912:SF23. Reduct_Se. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	896952.

Entry information

Entry name

TRXR1_CAEEL

Accession

Primary (citable) accession number: Q17745
Secondary accession number(s): Q9N2K1, Q9NJH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 26, 2008
Last modified:	December 14, 2011
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project